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基本情報
登録情報 | データベース: PDB / ID: 2j28 | ||||||
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タイトル | MODEL OF E. COLI SRP BOUND TO 70S RNCS | ||||||
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![]() | RIBOSOME / PROTEIN-RNA COMPLEX / SIGNAL RECOGNITION PARTICLE | ||||||
機能・相同性 | ![]() absorption of visible light / signal recognition particle / G protein-coupled opsin signaling pathway / photoreceptor inner segment membrane / G protein-coupled photoreceptor activity / 11-cis retinal binding / signal-recognition-particle GTPase / 7S RNA binding / SRP-dependent cotranslational protein targeting to membrane / protein targeting to membrane ...absorption of visible light / signal recognition particle / G protein-coupled opsin signaling pathway / photoreceptor inner segment membrane / G protein-coupled photoreceptor activity / 11-cis retinal binding / signal-recognition-particle GTPase / 7S RNA binding / SRP-dependent cotranslational protein targeting to membrane / protein targeting to membrane / photoreceptor outer segment membrane / negative regulation of cytoplasmic translational initiation / stringent response / transcriptional attenuation / positive regulation of ribosome biogenesis / endoribonuclease inhibitor activity / RNA-binding transcription regulator activity / translational termination / negative regulation of cytoplasmic translation / DnaA-L2 complex / translation repressor activity / negative regulation of DNA-templated DNA replication initiation / visual perception / mRNA regulatory element binding translation repressor activity / assembly of large subunit precursor of preribosome / ribosome assembly / cytosolic ribosome assembly / response to reactive oxygen species / translational initiation / regulation of cell growth / DNA-templated transcription termination / response to radiation / mRNA 5'-UTR binding / photoreceptor disc membrane / large ribosomal subunit / transferase activity / ribosome binding / 5S rRNA binding / ribosomal large subunit assembly / large ribosomal subunit rRNA binding / cytosolic large ribosomal subunit / cytoplasmic translation / tRNA binding / negative regulation of translation / rRNA binding / ribosome / structural constituent of ribosome / translation / ribonucleoprotein complex / response to antibiotic / negative regulation of DNA-templated transcription / GTPase activity / mRNA binding / GTP binding / ATP hydrolysis activity / DNA binding / RNA binding / zinc ion binding / metal ion binding / membrane / plasma membrane / cytosol / cytoplasm 類似検索 - 分子機能 | ||||||
生物種 | ![]() ![]() ![]() ![]() | ||||||
手法 | 電子顕微鏡法 / 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度: 9.5 Å | ||||||
![]() | Halic, M. / Blau, M. / Becker, T. / Mielke, T. / Pool, M.R. / Wild, K. / Sinning, I. / Beckmann, R. | ||||||
![]() | ![]() タイトル: Following the signal sequence from ribosomal tunnel exit to signal recognition particle. 著者: Mario Halic / Michael Blau / Thomas Becker / Thorsten Mielke / Martin R Pool / Klemens Wild / Irmgard Sinning / Roland Beckmann / ![]() 要旨: Membrane and secretory proteins can be co-translationally inserted into or translocated across the membrane. This process is dependent on signal sequence recognition on the ribosome by the signal ...Membrane and secretory proteins can be co-translationally inserted into or translocated across the membrane. This process is dependent on signal sequence recognition on the ribosome by the signal recognition particle (SRP), which results in targeting of the ribosome-nascent-chain complex to the protein-conducting channel at the membrane. Here we present an ensemble of structures at subnanometre resolution, revealing the signal sequence both at the ribosomal tunnel exit and in the bacterial and eukaryotic ribosome-SRP complexes. Molecular details of signal sequence interaction in both prokaryotic and eukaryotic complexes were obtained by fitting high-resolution molecular models. The signal sequence is presented at the ribosomal tunnel exit in an exposed position ready for accommodation in the hydrophobic groove of the rearranged SRP54 M domain. Upon ribosome binding, the SRP54 NG domain also undergoes a conformational rearrangement, priming it for the subsequent docking reaction with the NG domain of the SRP receptor. These findings provide the structural basis for improving our understanding of the early steps of co-translational protein sorting. | ||||||
履歴 |
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構造の表示
ムービー |
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構造ビューア | 分子: ![]() ![]() |
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ダウンロードとリンク
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ダウンロード
PDBx/mmCIF形式 | ![]() | 2.2 MB | 表示 | ![]() |
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PDB形式 | ![]() | 1.7 MB | 表示 | ![]() |
PDBx/mmJSON形式 | ![]() | ツリー表示 | ![]() | |
その他 | ![]() |
-検証レポート
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
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-関連構造データ
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リンク
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集合体
登録構造単位 | ![]()
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1 |
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要素
+50S ribosomal protein ... , 29種, 29分子 01234CDEFGHIJKLMNOPQRSTUVWXYZ
-RNA鎖 , 3種, 3分子 8AB
#7: RNA鎖 | 分子量: 23968.311 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() ![]() ![]() |
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#9: RNA鎖 | 分子量: 37848.555 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() ![]() ![]() |
#10: RNA鎖 | 分子量: 941612.375 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() ![]() ![]() |
-タンパク質・ペプチド / タンパク質 , 2種, 2分子 79
#6: タンパク質・ペプチド | 分子量: 2121.542 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() ![]() ![]() |
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#8: タンパク質 | 分子量: 47362.168 Da / 分子数: 1 / 由来タイプ: 組換発現 由来: (組換発現) ![]() ![]() 株: K12 / 遺伝子: FAZ83_22145 / 発現宿主: ![]() ![]() |
-非ポリマー , 2種, 623分子 


#35: 化合物 | ChemComp-MG / #36: 水 | ChemComp-HOH / | |
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-実験情報
-実験
実験 | 手法: 電子顕微鏡法 |
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EM実験 | 試料の集合状態: PARTICLE / 3次元再構成法: 単粒子再構成法 |
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試料調製
構成要素 | 名称: SRP BOUND TO 70S RNCS / タイプ: RIBOSOME |
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試料 | 包埋: NO / シャドウイング: NO / 染色: NO / 凍結: YES |
試料支持 | 詳細: CARBON |
急速凍結 | 凍結剤: ETHANE |
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電子顕微鏡撮影
実験機器 | ![]() モデル: Tecnai F30 / 画像提供: FEI Company |
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顕微鏡 | モデル: FEI TECNAI F30 |
電子銃 | 電子線源: ![]() |
電子レンズ | モード: BRIGHT FIELD |
撮影 | フィルム・検出器のモデル: KODAK SO-163 FILM |
放射波長 | 相対比: 1 |
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解析
EMソフトウェア | 名称: SPIDER / カテゴリ: 3次元再構成 | ||||||||||||
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対称性 | 点対称性: C1 (非対称) | ||||||||||||
3次元再構成 | 解像度: 9.5 Å / 解像度の算出法: FSC 0.5 CUT-OFF / 対称性のタイプ: POINT | ||||||||||||
精密化 | 最高解像度: 9.5 Å | ||||||||||||
精密化ステップ | サイクル: LAST / 最高解像度: 8 Å
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